6scp: Difference between revisions
No edit summary |
No edit summary |
||
| (One intermediate revision by the same user not shown) | |||
| Line 3: | Line 3: | ||
<StructureSection load='6scp' size='340' side='right'caption='[[6scp]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='6scp' size='340' side='right'caption='[[6scp]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6scp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SCP OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6scp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum_ATCC_13032 Corynebacterium glutamicum ATCC 13032]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SCP FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6scp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6scp OCA], [https://pdbe.org/6scp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6scp RCSB], [https://www.ebi.ac.uk/pdbsum/6scp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6scp ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8NNN6_CORGL Q8NNN6_CORGL] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The mechanisms of Z-ring assembly and regulation in bacteria are poorly understood, particularly in non-model organisms. Actinobacteria, a large bacterial phylum that includes the pathogen Mycobacterium tuberculosis, lack the canonical FtsZ-membrane anchors and Z-ring regulators described for E. coli. Here we investigate the physiological function of Corynebacterium glutamicum SepF, the only cell division-associated protein from Actinobacteria known to interact with the conserved C-terminal tail of FtsZ. We show an essential interdependence of FtsZ and SepF for formation of a functional Z-ring in C. glutamicum. The crystal structure of the SepF-FtsZ complex reveals a hydrophobic FtsZ-binding pocket, which defines the SepF homodimer as the functional unit, and suggests a reversible oligomerization interface. FtsZ filaments and lipid membranes have opposing effects on SepF polymerization, indicating that SepF has multiple roles at the cell division site, involving FtsZ bundling, Z-ring tethering and membrane reshaping activities that are needed for proper Z-ring assembly and function. | |||
Essential dynamic interdependence of FtsZ and SepF for Z-ring and septum formation in Corynebacterium glutamicum.,Sogues A, Martinez M, Gaday Q, Ben Assaya M, Grana M, Voegele A, VanNieuwenhze M, England P, Haouz A, Chenal A, Trepout S, Duran R, Wehenkel AM, Alzari PM Nat Commun. 2020 Apr 2;11(1):1641. doi: 10.1038/s41467-020-15490-8. PMID:32242019<ref>PMID:32242019</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6scp" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cell division protein 3D structures|Cell division protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Corynebacterium glutamicum ATCC 13032]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Alzari | [[Category: Alzari PM]] | ||
[[Category: Sogues | [[Category: Sogues A]] | ||
[[Category: Wehenkel | [[Category: Wehenkel AM]] | ||
Latest revision as of 15:39, 24 January 2024
Cell Division Protein SepF in complex with C-terminal domain of FtsZCell Division Protein SepF in complex with C-terminal domain of FtsZ
Structural highlights
FunctionPublication Abstract from PubMedThe mechanisms of Z-ring assembly and regulation in bacteria are poorly understood, particularly in non-model organisms. Actinobacteria, a large bacterial phylum that includes the pathogen Mycobacterium tuberculosis, lack the canonical FtsZ-membrane anchors and Z-ring regulators described for E. coli. Here we investigate the physiological function of Corynebacterium glutamicum SepF, the only cell division-associated protein from Actinobacteria known to interact with the conserved C-terminal tail of FtsZ. We show an essential interdependence of FtsZ and SepF for formation of a functional Z-ring in C. glutamicum. The crystal structure of the SepF-FtsZ complex reveals a hydrophobic FtsZ-binding pocket, which defines the SepF homodimer as the functional unit, and suggests a reversible oligomerization interface. FtsZ filaments and lipid membranes have opposing effects on SepF polymerization, indicating that SepF has multiple roles at the cell division site, involving FtsZ bundling, Z-ring tethering and membrane reshaping activities that are needed for proper Z-ring assembly and function. Essential dynamic interdependence of FtsZ and SepF for Z-ring and septum formation in Corynebacterium glutamicum.,Sogues A, Martinez M, Gaday Q, Ben Assaya M, Grana M, Voegele A, VanNieuwenhze M, England P, Haouz A, Chenal A, Trepout S, Duran R, Wehenkel AM, Alzari PM Nat Commun. 2020 Apr 2;11(1):1641. doi: 10.1038/s41467-020-15490-8. PMID:32242019[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||